Ulex europaeus Lectin (UEA II) - Pure

Affinity purified Ulex europaeus agglutinin (UEA II) is a glycoprotein isolated from gorse seeds, composed of four 24,000 Da monomer subunits that require Ca²âº for ligand binding via its carbohydrate recognition domain. It specifically binds to di-N-acetylchitobiose, an oligomer of GlcNAc, while GlcNAc itself does not inhibit its activity. UEA II has no mitogenic activity and agglutinates type O erythrocytes more effectively than type A3. Agglutinating activity is lost with EDTA but can be restored by adding calcium. Additionally, UEA II inhibits the lectin complement pathway after endothelial oxidative stress, likely through competition for a binding site on endothelial cells, rather than inhibiting mannose-binding lectin (MBL).

Recommended Usage: Recommended dilutions of 0.5 – 20 μg/ml in 20 mM Tris-HCl pH 7.5, 50 mM NaCl, 1 mM CaCl2, 0.5 mM MnCl2. 5 – 20 μg/ml of UEA II can agglutinate type O erythrocytes.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Immunohistochemistry, Immunocytochemistry, Bioconjugations, Blotting, ELISA, Cell typing, Glycobiology.

References

1. Horejsí V. Properties of Ulex europaeus II lectin isolated by affinity chromatography. Biochim Biophys Acta. 1979 Apr 25;577(2):389-93.
2. Allen HJ, Johnson EA. A simple procedure for the isolation of L-fucose-binding lectins from Ulex europaeus and Lotus tetragonolobus. Carbohydr Res. 1977 Oct;58(2):253-65.
3. Loris R, De Greve H, Dao-Thi MH, Messens J, Imberty A, Wyns L. Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site. J Mol Biol. 2000 Aug 25;301(4):987-1002.